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Science 12 December 1986:
Vol. 234. no. 4782, pp. 1395 - 1398
DOI: 10.1126/science.2431483
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Articles

Science, Vol 234, Issue 4782, 1395-1398
Copyright © 1986 by American Association for the Advancement of Science

articles

Oligodendrocyte adhesion activates protein kinase C-mediated phosphorylation of myelin basic protein

T Vartanian, S Szuchet, G Dawson, and AT Campagnoni

When isolated adult oligodendrocytes adhere to a substratum myelinogenesis occurs. Investigation of the mechanism by which this happens indicated that the oligodendrocyte-substratum interaction activated protein kinase C-dependent phosphorylation of myelin basic protein and promoted the synthesis of myelin basic protein. In addition, when agents that activate protein kinase C (second messenger diacylglycerol or a tumor-promoting phorbol ester) were added to nonattached oligodendrocytes, they mimicked the influence of the substratum by inducing phosphorylation of myelin basic protein; and reagents that increase cellular adenosine 3', 5'-monophosphate (cyclic AMP) inhibited phosphorylation of myelin basic protein. Thus, at least in vitro, the interaction between oligodendrocytes and the substratum may mediate myelinogenic events, and phosphorylation of myelin basic protein may be an early requirement in the sequence of steps that ultimately results in myelin formation.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Identification and Characterization of Oligodendrocyte Thromboxane A2 Receptors.
S. C. Blackman, G. Dawson, K. Antonakis, and G. C. Le Breton (1998)
J. Biol. Chem. 273, 475-483
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